Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7EKQ

CrClpP-S2c

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004176	molecular_function	ATP-dependent peptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
B	0004176	molecular_function	ATP-dependent peptidase activity
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
B	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0009368	cellular_component	endopeptidase Clp complex
B	0009536	cellular_component	plastid
B	0016787	molecular_function	hydrolase activity
B	0051117	molecular_function	ATPase binding
C	0004176	molecular_function	ATP-dependent peptidase activity
C	0004252	molecular_function	serine-type endopeptidase activity
C	0006508	biological_process	proteolysis
D	0004176	molecular_function	ATP-dependent peptidase activity
D	0004252	molecular_function	serine-type endopeptidase activity
D	0006508	biological_process	proteolysis
D	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
D	0008233	molecular_function	peptidase activity
D	0008236	molecular_function	serine-type peptidase activity
D	0009368	cellular_component	endopeptidase Clp complex
D	0009536	cellular_component	plastid
D	0016787	molecular_function	hydrolase activity
D	0051117	molecular_function	ATPase binding
E	0004176	molecular_function	ATP-dependent peptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
F	0004176	molecular_function	ATP-dependent peptidase activity
F	0004252	molecular_function	serine-type endopeptidase activity
F	0006508	biological_process	proteolysis
F	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
F	0008233	molecular_function	peptidase activity
F	0008236	molecular_function	serine-type peptidase activity
F	0009368	cellular_component	endopeptidase Clp complex
F	0009536	cellular_component	plastid
F	0016787	molecular_function	hydrolase activity
F	0051117	molecular_function	ATPase binding
G	0004176	molecular_function	ATP-dependent peptidase activity
G	0004252	molecular_function	serine-type endopeptidase activity
G	0006508	biological_process	proteolysis
H	0004176	molecular_function	ATP-dependent peptidase activity
H	0004252	molecular_function	serine-type endopeptidase activity
H	0006508	biological_process	proteolysis
I	0004176	molecular_function	ATP-dependent peptidase activity
I	0004252	molecular_function	serine-type endopeptidase activity
I	0006508	biological_process	proteolysis
J	0004176	molecular_function	ATP-dependent peptidase activity
J	0004252	molecular_function	serine-type endopeptidase activity
J	0006508	biological_process	proteolysis
K	0004176	molecular_function	ATP-dependent peptidase activity
K	0004252	molecular_function	serine-type endopeptidase activity
K	0006508	biological_process	proteolysis
K	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
K	0009368	cellular_component	endopeptidase Clp complex
K	0009536	cellular_component	plastid
K	0051117	molecular_function	ATPase binding
L	0004176	molecular_function	ATP-dependent peptidase activity
L	0004252	molecular_function	serine-type endopeptidase activity
L	0006508	biological_process	proteolysis
M	0004176	molecular_function	ATP-dependent peptidase activity
M	0004252	molecular_function	serine-type endopeptidase activity
M	0006508	biological_process	proteolysis
N	0004176	molecular_function	ATP-dependent peptidase activity
N	0004252	molecular_function	serine-type endopeptidase activity
N	0006508	biological_process	proteolysis
N	0006515	biological_process	protein quality control for misfolded or incompletely synthesized proteins
N	0009368	cellular_component	endopeptidase Clp complex
N	0009536	cellular_component	plastid
N	0051117	molecular_function	ATPase binding
P	0005524	molecular_function	ATP binding
P	0006457	biological_process	protein folding
P	0044183	molecular_function	protein folding chaperone
Q	0005524	molecular_function	ATP binding
Q	0006457	biological_process	protein folding
Q	0044183	molecular_function	protein folding chaperone
R	0005524	molecular_function	ATP binding
R	0005739	cellular_component	mitochondrion
R	0006457	biological_process	protein folding
R	0009507	cellular_component	chloroplast
R	0044183	molecular_function	protein folding chaperone
R	0046872	molecular_function	metal ion binding
R	0051082	molecular_function	unfolded protein binding
R	0051087	molecular_function	protein-folding chaperone binding
S	0005524	molecular_function	ATP binding
S	0005739	cellular_component	mitochondrion
S	0006457	biological_process	protein folding
S	0009507	cellular_component	chloroplast
S	0044183	molecular_function	protein folding chaperone
S	0046872	molecular_function	metal ion binding
S	0051082	molecular_function	unfolded protein binding
S	0051087	molecular_function	protein-folding chaperone binding

Functional Information from PROSITE/UniProt

site_id	PS00681
Number of Residues	25
Details	CHAPERONINS_CPN10 Chaperonins cpn10 signature. LkPLsDRILIKgakaedktsGgVLL

Chain	Residue	Details
R	LEU101-LEU125
P	MET16-LEU40
Q	LEU118-LEU142

site_id	PS00381
Number of Residues	12
Details	CLP_PROTEASE_SER Endopeptidase Clp serine active site. TccIGlAASMGA

Chain	Residue	Details
B	THR123-ALA134
H	THR378-SER389
C	THR87-ALA98

site_id	PS00382
Number of Residues	14
Details	CLP_PROTEASE_HIS Endopeptidase Clp histidine active site. RyslPnsrIMIHQP

Chain	Residue	Details
B	ARG145-PRO158
H	ARG400-PRO413
C	ARG109-PRO122

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10085","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10086","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	3
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)